Crystallization and preliminary X-ray analysis of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter nitroguajacolicus Ru61a:: a cofactor-devoid dioxygenase of the α/β-hydrolase-fold superfamily

被引：7
|
作者：
Steiner, Roberto A.
Frerichs-Deeken, Ursula
Fetzner, Susanne
机构：
[1] Kings Coll London, Randall Div Cell & Mol Biophys, London SE1 1UL, England
[2] Univ Munster, Inst Mol Mikrobiol & Biotechnol, D-48149 Munster, Germany
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2007年 / 63卷
关键词：
D O I：
10.1107/S174430910701353X
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) is a cofactor-devoid dioxygenase that is involved in the anthranilate pathway of quinaldine degradation. HOD has been proposed to belong to the alpha/beta-hydrolase-fold superfamily of enzymes. N-terminally His(6)-tagged HOD has been crystallized by the hanging-drop vapour-diffusion method using sodium/potassium tartrate as a precipitant and CuCl2 as an additive. The structure was solved by the single anomalous dispersion (SAD) technique using data collected to 3.5 angstrom resolution at the Cu absorption peak wavelength. The crystals belong to the primitive tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 153.788, c=120.872 angstrom.
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页码：382 / 385
页数：4
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